Fig. 2: Selectivity within the ZUFSP family.
From: A structural basis for the diverse linkage specificities within the ZUFSP deubiquitinase family
a Schematic representation of the domain architecture of ZUP1 homologs from different species. UBZ-like zinc fingers (Z), MIU domains (M), ZUFSP ubiquitin-binding domains (zUBD), α-2/3 region, and the catalytic domain are shown as boxes. The position of the non-conserved α-2/3 region in insect ZUP is indicated by a dashed line. b, c Activity of ZUP homologs from A. thaliana (AtZUP) and T. castaneum (TcZUP) against RLRGG-AMC (b) and ubiquitin-AMC (c). The RFU values shown are the means of triplicates. d, e Linkage specificity analysis of AtZUP. A panel of di-ubiquitin (d) or tetra-ubiquitin (e) chains was treated with GST-AtZUP for the indicated time points. Black arrowheads mark the N- and C-terminal fragments of AtZUP (Supplementary Fig. 5c). f, g Linkage specificity analysis of TcZUP. A panel of di-ubiquitin (f) or tetra-ubiquitin (g) chains was treated with TcZUP for the indicated time points. h Comparison of ZUP1 and TcZUP hydrolysis rate. K63-linked di-ubiquitin was treated with ZUP1 or TcZUP for the indicated time points. Source data are provided as a Source Data file.
